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NOL_ARATH
ID   NOL_ARATH               Reviewed;         348 AA.
AC   Q8LEU3; Q9FF83;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Chlorophyll(ide) b reductase NOL, chloroplastic;
DE            EC=1.1.1.294;
DE   AltName: Full=Protein NON-YELLOW COLORING 1-LIKE;
DE            Short=AtNOL;
DE            Short=Protein NYC1-LIKE;
DE   AltName: Full=Short-chain dehydrogenase/reductase NOL;
DE   Flags: Precursor;
GN   Name=NOL; OrderedLocusNames=At5g04900; ORFNames=MUG13.25;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=17416733; DOI=10.1105/tpc.106.042911;
RA   Kusaba M., Ito H., Morita R., Iida S., Sato Y., Fujimoto M., Kawasaki S.,
RA   Tanaka R., Hirochika H., Nishimura M., Tanaka A.;
RT   "Rice NON-YELLOW COLORING1 is involved in light-harvesting complex II and
RT   grana degradation during leaf senescence.";
RL   Plant Cell 19:1362-1375(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=19403948; DOI=10.1074/jbc.m109.008912;
RA   Horie Y., Ito H., Kusaba M., Tanaka R., Tanaka A.;
RT   "Participation of chlorophyll b reductase in the initial step of the
RT   degradation of light-harvesting chlorophyll a/b-protein complexes in
RT   Arabidopsis.";
RL   J. Biol. Chem. 284:17449-17456(2009).
RN   [7]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH NYC1; RCCR AND LHCII COMPLEX.
RX   PubMed=22366162; DOI=10.1105/tpc.111.089474;
RA   Sakuraba Y., Schelbert S., Park S.Y., Han S.H., Lee B.D., Andres C.B.,
RA   Kessler F., Hortensteiner S., Paek N.C.;
RT   "STAY-GREEN and chlorophyll catabolic enzymes interact at light-harvesting
RT   complex II for chlorophyll detoxification during leaf senescence in
RT   Arabidopsis.";
RL   Plant Cell 24:507-518(2012).
RN   [8]
RP   INTERACTION WITH HCAR, AND DEVELOPMENTAL STAGE.
RX   PubMed=23200839; DOI=10.1016/j.bbrc.2012.11.050;
RA   Sakuraba Y., Kim Y.S., Yoo S.C., Hortensteiner S., Paek N.C.;
RT   "7-Hydroxymethyl chlorophyll a reductase functions in metabolic channeling
RT   of chlorophyll breakdown intermediates during leaf senescence.";
RL   Biochem. Biophys. Res. Commun. 430:32-37(2013).
CC   -!- FUNCTION: Required for chlorophyll b degradation. Chlorophyll b,
CC       chlorophyllide b, pheophorbide b and pheophytin b can be used as
CC       substrates. Belongs to the chlorophyll catabolic enzymes (CCEs).
CC       {ECO:0000269|PubMed:19403948}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7(1)-hydroxychlorophyllide a + NAD(+) = chlorophyllide b +
CC         H(+) + NADH; Xref=Rhea:RHEA:24768, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83356,
CC         ChEBI:CHEBI:83357; EC=1.1.1.294;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7(1)-hydroxychlorophyllide a + NADP(+) = chlorophyllide b +
CC         H(+) + NADPH; Xref=Rhea:RHEA:24772, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83356,
CC         ChEBI:CHEBI:83357; EC=1.1.1.294;
CC   -!- SUBUNIT: Interacts with NCY1 to form a complex that acts as a
CC       chlorophyll b reductase. Interacts with HCAR, RCCR and the LHCII
CC       complex. Part of a SGR1-CCE-LHCII complex, which acts in chlorophyll
CC       breakdown. {ECO:0000269|PubMed:22366162, ECO:0000269|PubMed:23200839}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:22366162}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:22366162}.
CC   -!- DEVELOPMENTAL STAGE: Constantly expressed throughout development.
CC       {ECO:0000269|PubMed:23200839}.
CC   -!- DISRUPTION PHENOTYPE: Slower degradation of chlorophyll b during dark
CC       incubation. {ECO:0000269|PubMed:19403948}.
CC   -!- MISCELLANEOUS: Chlorophyll b reductase activity detected in vitro with
CC       a recombinant protein produced in a heterologous system. Able to act on
CC       the substrate within the protein-chlorophyll LHCII complex.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB11512.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB255027; BAF49742.1; -; mRNA.
DR   EMBL; AB005245; BAB11512.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED90802.1; -; Genomic_DNA.
DR   EMBL; AY085229; AAM62462.1; -; mRNA.
DR   EMBL; BT025238; ABF18991.1; -; mRNA.
DR   RefSeq; NP_568145.1; NM_120572.3.
DR   AlphaFoldDB; Q8LEU3; -.
DR   SMR; Q8LEU3; -.
DR   BioGRID; 15651; 7.
DR   IntAct; Q8LEU3; 2.
DR   MINT; Q8LEU3; -.
DR   STRING; 3702.AT5G04900.1; -.
DR   PaxDb; Q8LEU3; -.
DR   PRIDE; Q8LEU3; -.
DR   ProteomicsDB; 250594; -.
DR   EnsemblPlants; AT5G04900.1; AT5G04900.1; AT5G04900.
DR   GeneID; 830372; -.
DR   Gramene; AT5G04900.1; AT5G04900.1; AT5G04900.
DR   KEGG; ath:AT5G04900; -.
DR   Araport; AT5G04900; -.
DR   TAIR; locus:2175254; AT5G04900.
DR   eggNOG; KOG0725; Eukaryota.
DR   HOGENOM; CLU_010194_2_4_1; -.
DR   InParanoid; Q8LEU3; -.
DR   OMA; RWINNAG; -.
DR   OrthoDB; 1190834at2759; -.
DR   PhylomeDB; Q8LEU3; -.
DR   BioCyc; ARA:AT5G04900-MON; -.
DR   BioCyc; MetaCyc:AT5G04900-MON; -.
DR   BRENDA; 1.1.1.294; 399.
DR   PRO; PR:Q8LEU3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8LEU3; baseline and differential.
DR   Genevisible; Q8LEU3; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0034256; F:chlorophyll(ide) b reductase activity; IDA:TAIR.
DR   GO; GO:0015996; P:chlorophyll catabolic process; IDA:TAIR.
DR   GO; GO:0010304; P:PSII associated light-harvesting complex II catabolic process; TAS:TAIR.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Chlorophyll catabolism; Chloroplast; Membrane; NAD; Oxidoreductase;
KW   Plastid; Reference proteome; Thylakoid; Transit peptide.
FT   TRANSIT         1..61
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           62..348
FT                   /note="Chlorophyll(ide) b reductase NOL, chloroplastic"
FT                   /id="PRO_0000391416"
FT   ACT_SITE        233
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         84..108
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   348 AA;  38149 MW;  B008E8957D3B2CB7 CRC64;
     MATWSGFNVS SSPLLRLRSS SVSNVTKLPF LSPICRRRLL AERFGLATVV VTRQNLTVTP
     SSAAVEARIS GKREPMTPPY NILITGSTKG IGYALAREFL KAGDNVVICS RSAERVETAV
     QSLKEEFGEH VWGTKCDVTE GKDVRELVAY SQKNLKYIDI WINNAGSNAY SFKPLAEASD
     EDLIEVVKTN TLGLMLCCRE AMNMMLTQSR GGHIFNIDGA GSDGRPTPRF AAYGATKRSV
     VHLTKSLQAE LQMQDVKNVV VHNLSPGMVT TDLLMSGATT KQAKFFINVL AEPAEVVAEY
     LVPNIRAIPA SGSMKPTYIR FLTGIKAYTK IFSRVALGAR KNRYVTEE
 
 
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